K
Kari Alitalo
Researcher at University of Helsinki
Publications - 844
Citations - 122462
Kari Alitalo is an academic researcher from University of Helsinki. The author has contributed to research in topics: Angiogenesis & Vascular endothelial growth factor C. The author has an hindex of 174, co-authored 817 publications receiving 114231 citations. Previous affiliations of Kari Alitalo include Mount Sinai Hospital, Toronto & Cornell University.
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Expression of FGFR-4 mRNA in developing mouse tissues.
TL;DR: The cloned mouse FGFR-4 cDNA is cloned and used in Northern and in situ hybridization of mouse embryonic tissues, and results suggest that FG FR-4 may be particularly important for the differentiation of skeletal muscle and endodermally derived organs.
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Endothelial Bmx tyrosine kinase activity is essential for myocardial hypertrophy and remodeling.
Tanja Holopainen,Markus Räsänen,Andrey Anisimov,Tomi Tuomainen,Wei Zheng,Denis Tvorogov,Juha J. Hulmi,Leif C. Andersson,Bruno Cenni,Pasi Tavi,Eero Mervaala,Riikka Kivelä,Kari Alitalo +12 more
TL;DR: The results show that the kinase activity of the endothelial bone marrow kinase in chromosome X (Bmx) protein is necessary for the development of pathological cardiac hypertrophy, and suggest that the endothelium Bmx tyrosine kinase could provide a target to attenuate theDevelopment of cardiachypertrophy.
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Myc protein: partners and antagonists
TL;DR: Results suggest that the Myc/Max heterodimer functions as a transcriptional activator of genes that are critical for the regulation of cell growth.
Journal Article
The human ryk cDNA sequence predicts a protein containing two putative transmembrane segments and a tyrosine kinase catalytic domain.
Luca Tamagnone,Juha Partanen,Elina Armstrong,Jerzy Lasota,Kinya Ohgami,Tetsushi Tazunoki,Sal LaForgia,Kay Huebner,Kari Alitalo +8 more
TL;DR: The open reading frame of human ryk encodes a novel type of putative tyrosine kinase of 607 amino acid residues, having two potential transmembrane domains and homology to receptor tyrosin kinases, such as met (HGF/SF-R) and IGF-1R, in its catalytic domain.
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Identification of csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure.
TL;DR: It is shown that human Csk is tyrosine phosphorylated in HeLa cells treated with sodium pervanadate and three-dimensional modelling of the Csk kinase domain indicated that the Y304F mutation abolishes one of two conserved hydrogen bonds between the upper and the lower lobes in the open conformation of the kinasedomain.